hrp conjugated secondary antibodies  (Jackson Immuno)

 
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    Peroxidase AffiniPure F ab ₂ Fragment Goat Anti Human Serum IgA α chain specific
    Description:
    F ab 2 fragment antibodies are generated by pepsin digestion of whole IgG antibodies to remove most of the Fc region while leaving some of the hinge region F ab 2 fragments have two antigen binding Fab portions linked together by disulfide bonds and therefore they are divalent The average molecular weight is about 110 kDa They are used for specific applications such as to avoid binding of secondary antibodies to live cells with Fc receptors or to Protein A or Protein G Based on immunoelectrophoresis and or ELISA the antibody reacts with the heavy chain of human IgA but not with human IgG or IgM No antibody was detected against non immunoglobulin serum proteins The antibody may cross react with IgA from other species
    Catalog Number:
    109-036-011
    Price:
    141.0
    Category:
    F ab ₂ Fragment Affinity Purified Antibodies
    Conjugate:
    Horseradish Peroxidase
    Size:
    0 5 ml
    Format:
    F(ab')₂ Fragment
    Host:
    Goat
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    Structured Review

    Jackson Immuno hrp conjugated secondary antibodies
    Independent diffusion of SV proteins following nerve stimulation is sustained for long periods following LAP inactivation Third instar larval NMJ preparations from the indicated genotypes were dissected, incubated with FlAsH-EDT 2 and muscle 4 from segment A2 or A3 was exposed to 488-nm-filtered fluorescent light for 5 min. Clap4C; lap = Clap4C; lap 1 /lap sd3 . Following illumination, the larval NMJs were stimulated continuously with high K + (90 m m ) Jan's solution for 5 min (A and B) or 30 min (C and D) or 10 min (E and F). Following nerve stimulation, the larvae were washed rapidly with Ca 2+ -free HL-3 saline and fixed. The NMJs were then stained for a pair of SV proteins Syn and vGlut or Syt1 and <t>CSP.</t> Panels A–D also show <t>HRP-stained</t> NMJs (blue) to mark the neuronal membrane. The stimulation paradigm does not affect SV protein colocalization in wild-type control larval NMJs in which most SV proteins are colocalized although we note that not all SV proteins are fully colocalized even in the wild-type larval NMJs. In contrast, there are more punctate in LAP-inactivated synaptic boutons and SV proteins are often not colocalized in these punctate (arrows). G and H) Following 10 min of stimulation with high K + , nerve terminals were allowed to rest in Ca 2+ -free HL-3 saline for an additional 20 min prior to fixation. Following the resting period, dramatically large punctate can be observed positive for both Syt1 and Syn (arrowheads) in larval NMJs whose LAP is inactivated, while some portions of the punctate within the bouton are positive for only one of the two SV proteins (arrows). The protocol for both control and experimental samples was identical. Scale bars = 10 µm.
    F ab 2 fragment antibodies are generated by pepsin digestion of whole IgG antibodies to remove most of the Fc region while leaving some of the hinge region F ab 2 fragments have two antigen binding Fab portions linked together by disulfide bonds and therefore they are divalent The average molecular weight is about 110 kDa They are used for specific applications such as to avoid binding of secondary antibodies to live cells with Fc receptors or to Protein A or Protein G Based on immunoelectrophoresis and or ELISA the antibody reacts with the heavy chain of human IgA but not with human IgG or IgM No antibody was detected against non immunoglobulin serum proteins The antibody may cross react with IgA from other species
    https://www.bioz.com/result/hrp conjugated secondary antibodies/product/Jackson Immuno
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hrp conjugated secondary antibodies - by Bioz Stars, 2021-07
    99/100 stars

    Images

    1) Product Images from "AP180 Couples Protein Retrieval to Clathrin-Mediated Endocytosis of Synaptic Vesicles"

    Article Title: AP180 Couples Protein Retrieval to Clathrin-Mediated Endocytosis of Synaptic Vesicles

    Journal: Traffic (Copenhagen, Denmark)

    doi: 10.1111/tra.12153

    Independent diffusion of SV proteins following nerve stimulation is sustained for long periods following LAP inactivation Third instar larval NMJ preparations from the indicated genotypes were dissected, incubated with FlAsH-EDT 2 and muscle 4 from segment A2 or A3 was exposed to 488-nm-filtered fluorescent light for 5 min. Clap4C; lap = Clap4C; lap 1 /lap sd3 . Following illumination, the larval NMJs were stimulated continuously with high K + (90 m m ) Jan's solution for 5 min (A and B) or 30 min (C and D) or 10 min (E and F). Following nerve stimulation, the larvae were washed rapidly with Ca 2+ -free HL-3 saline and fixed. The NMJs were then stained for a pair of SV proteins Syn and vGlut or Syt1 and CSP. Panels A–D also show HRP-stained NMJs (blue) to mark the neuronal membrane. The stimulation paradigm does not affect SV protein colocalization in wild-type control larval NMJs in which most SV proteins are colocalized although we note that not all SV proteins are fully colocalized even in the wild-type larval NMJs. In contrast, there are more punctate in LAP-inactivated synaptic boutons and SV proteins are often not colocalized in these punctate (arrows). G and H) Following 10 min of stimulation with high K + , nerve terminals were allowed to rest in Ca 2+ -free HL-3 saline for an additional 20 min prior to fixation. Following the resting period, dramatically large punctate can be observed positive for both Syt1 and Syn (arrowheads) in larval NMJs whose LAP is inactivated, while some portions of the punctate within the bouton are positive for only one of the two SV proteins (arrows). The protocol for both control and experimental samples was identical. Scale bars = 10 µm.
    Figure Legend Snippet: Independent diffusion of SV proteins following nerve stimulation is sustained for long periods following LAP inactivation Third instar larval NMJ preparations from the indicated genotypes were dissected, incubated with FlAsH-EDT 2 and muscle 4 from segment A2 or A3 was exposed to 488-nm-filtered fluorescent light for 5 min. Clap4C; lap = Clap4C; lap 1 /lap sd3 . Following illumination, the larval NMJs were stimulated continuously with high K + (90 m m ) Jan's solution for 5 min (A and B) or 30 min (C and D) or 10 min (E and F). Following nerve stimulation, the larvae were washed rapidly with Ca 2+ -free HL-3 saline and fixed. The NMJs were then stained for a pair of SV proteins Syn and vGlut or Syt1 and CSP. Panels A–D also show HRP-stained NMJs (blue) to mark the neuronal membrane. The stimulation paradigm does not affect SV protein colocalization in wild-type control larval NMJs in which most SV proteins are colocalized although we note that not all SV proteins are fully colocalized even in the wild-type larval NMJs. In contrast, there are more punctate in LAP-inactivated synaptic boutons and SV proteins are often not colocalized in these punctate (arrows). G and H) Following 10 min of stimulation with high K + , nerve terminals were allowed to rest in Ca 2+ -free HL-3 saline for an additional 20 min prior to fixation. Following the resting period, dramatically large punctate can be observed positive for both Syt1 and Syn (arrowheads) in larval NMJs whose LAP is inactivated, while some portions of the punctate within the bouton are positive for only one of the two SV proteins (arrows). The protocol for both control and experimental samples was identical. Scale bars = 10 µm.

    Techniques Used: Diffusion-based Assay, Incubation, Staining

    2) Product Images from "Accumulation of rab4GTP in the Cytoplasm and Association with the Peptidyl-Prolyl Isomerase Pin1 during Mitosis"

    Article Title: Accumulation of rab4GTP in the Cytoplasm and Association with the Peptidyl-Prolyl Isomerase Pin1 during Mitosis

    Journal: Molecular Biology of the Cell

    doi:

    Released rab4 is not associated with GDI. Equal numbers of interphase (I) and mitotic (M) rab4/HisGDI CHO double transfectants and control rab4 CHO cells were homogenized and fractionated by high speed centrifugation. Cytosol was retrieved and incubated with 50 μl Ni-NTA beads. Beads were washed three times with ice-cold RIPA buffer and boiled in Laemmli sample buffer. Eluted proteins were separated by SDS-PAGE and analyzed by Western blot using the anti Xpress antibody for HisGDI and a rabbit rab4 antibody. Detection was with HRP-labeled secondary antibodies and enhanced chemiluminescence. Quantitation was done using the NIH image software package (A). Mitotic rab4/HisGDI CHO double transfectants were labeled 45 min with 500 μCi/ml 32 P ortho phosphate. Cells were lysed in 1% octylglucoside as described in MATERIALS AND METHODS. Equal aliquots cleared lysate were incubated for 1 h with a GDI antibody (+) or preimmune serum (-) adsorbed to Protein A Sepharose CL-4B and washed 3 times with octylglucoside wash buffer. Washed immunoprecipitates were boiled 5 min with 100 μl 0.5% SDS in PBS and pelleted. Supernatants were used to immunoprecipitate rab4 as described inMATERIALS AND METHODS, resolved on 12.5% SDS PAA mini gels, and analyzed by phosphorimaging (B).
    Figure Legend Snippet: Released rab4 is not associated with GDI. Equal numbers of interphase (I) and mitotic (M) rab4/HisGDI CHO double transfectants and control rab4 CHO cells were homogenized and fractionated by high speed centrifugation. Cytosol was retrieved and incubated with 50 μl Ni-NTA beads. Beads were washed three times with ice-cold RIPA buffer and boiled in Laemmli sample buffer. Eluted proteins were separated by SDS-PAGE and analyzed by Western blot using the anti Xpress antibody for HisGDI and a rabbit rab4 antibody. Detection was with HRP-labeled secondary antibodies and enhanced chemiluminescence. Quantitation was done using the NIH image software package (A). Mitotic rab4/HisGDI CHO double transfectants were labeled 45 min with 500 μCi/ml 32 P ortho phosphate. Cells were lysed in 1% octylglucoside as described in MATERIALS AND METHODS. Equal aliquots cleared lysate were incubated for 1 h with a GDI antibody (+) or preimmune serum (-) adsorbed to Protein A Sepharose CL-4B and washed 3 times with octylglucoside wash buffer. Washed immunoprecipitates were boiled 5 min with 100 μl 0.5% SDS in PBS and pelleted. Supernatants were used to immunoprecipitate rab4 as described inMATERIALS AND METHODS, resolved on 12.5% SDS PAA mini gels, and analyzed by phosphorimaging (B).

    Techniques Used: Centrifugation, Incubation, SDS Page, Western Blot, Labeling, Quantitation Assay, Software

    Rab4 is in a complex with Pin1 in cytosol during mitosis. Equal numbers of interphase and mitotic rab4/HisPin1 CHO double transfectants and rab4 CHO cells (A, B), or rab4S196Q and rab4S196Q/HisPin1 CHO transfectants (B) were homogenized and fractionated by high speed centrifugation. Cytosol was retrieved and incubated with 50 μl Ni-NTA beads. Beads were washed three times with ice-cold RIPA buffer and boiled in Laemmli sample buffer. Eluted proteins were separated by SDS-PAGE and analyzed by Western blot using the Xpress antibody for HisPin1 and a rabbit rab4 antibody. Detection was done with HRP-labeled secondary antibodies and enhanced chemiluminescence and quantitated using the NIH image software package.
    Figure Legend Snippet: Rab4 is in a complex with Pin1 in cytosol during mitosis. Equal numbers of interphase and mitotic rab4/HisPin1 CHO double transfectants and rab4 CHO cells (A, B), or rab4S196Q and rab4S196Q/HisPin1 CHO transfectants (B) were homogenized and fractionated by high speed centrifugation. Cytosol was retrieved and incubated with 50 μl Ni-NTA beads. Beads were washed three times with ice-cold RIPA buffer and boiled in Laemmli sample buffer. Eluted proteins were separated by SDS-PAGE and analyzed by Western blot using the Xpress antibody for HisPin1 and a rabbit rab4 antibody. Detection was done with HRP-labeled secondary antibodies and enhanced chemiluminescence and quantitated using the NIH image software package.

    Techniques Used: Centrifugation, Incubation, SDS Page, Western Blot, Labeling, Software

    3) Product Images from "Components of an SCF ubiquitin ligase localize to the centrosome and regulate the centrosome duplication cycle"

    Article Title: Components of an SCF ubiquitin ligase localize to the centrosome and regulate the centrosome duplication cycle

    Journal: Genes & Development

    doi:

    Skp1 is pericentriolar in purified centrosomes and in NIH-3T3 cells. Centrosomes were purified from CHO cells and prepared for immunofluorescence as described (see Materials and Methods). ( A ) Centrosomes spun onto coverslips were fixed in methanol and labeled with mouse monoclonal antibodies against α-tubulin and affinity-purified rabbit antibodies against Skp1, followed by secondary antibodies. Anti-α-tubulin (green); Anti-Skp1 (red). ( B ) Immunoblotting detects Skp1 in a purified centrosome sample. An NIH-3T3 cell lysate (lanes 1,3 ) and a centrosome sample (lanes 2,4 ) were subjected to Western blotting with either affinity-purified anti-Skp1 antibodies (lanes 1,2 ) or rabbit antibodies to γ-tubulin (lanes 3,4 ). Secondary antibody was HRP-conjugated donkey anti-rabbit IgG and bands were detected with ECL reagents as above. Skp1 and γ-tubulin are indicated (arrows). Molecular mass markers are as indicated. ( C ) NIH-3T3 cells fixed in methanol, and labeled using a mouse mAb against γ-tubulin and with rabbit affinity-purified anti-Skp1 antibodies followed by secondary antibodies. Anti-γ-tubulin (green); anti-Skp1 (red). Deconvolution images of centrosomes in cells at different phases of the cell cycle are pictured ( left to right ).
    Figure Legend Snippet: Skp1 is pericentriolar in purified centrosomes and in NIH-3T3 cells. Centrosomes were purified from CHO cells and prepared for immunofluorescence as described (see Materials and Methods). ( A ) Centrosomes spun onto coverslips were fixed in methanol and labeled with mouse monoclonal antibodies against α-tubulin and affinity-purified rabbit antibodies against Skp1, followed by secondary antibodies. Anti-α-tubulin (green); Anti-Skp1 (red). ( B ) Immunoblotting detects Skp1 in a purified centrosome sample. An NIH-3T3 cell lysate (lanes 1,3 ) and a centrosome sample (lanes 2,4 ) were subjected to Western blotting with either affinity-purified anti-Skp1 antibodies (lanes 1,2 ) or rabbit antibodies to γ-tubulin (lanes 3,4 ). Secondary antibody was HRP-conjugated donkey anti-rabbit IgG and bands were detected with ECL reagents as above. Skp1 and γ-tubulin are indicated (arrows). Molecular mass markers are as indicated. ( C ) NIH-3T3 cells fixed in methanol, and labeled using a mouse mAb against γ-tubulin and with rabbit affinity-purified anti-Skp1 antibodies followed by secondary antibodies. Anti-γ-tubulin (green); anti-Skp1 (red). Deconvolution images of centrosomes in cells at different phases of the cell cycle are pictured ( left to right ).

    Techniques Used: Purification, Immunofluorescence, Labeling, Affinity Purification, Western Blot

    A Nedd8-modified form of Cul1 is present at the centrosome. ( A ) NIH-3T3 cells were grown on cover slips, fixed in methanol and labeled with affinity-purified antibodies against the amino-terminal portion of human Cul1 and with human anti-centrosome antiserum, followed by secondary antibodies and Hoechst dye. Cul1 staining is shown at the centrosome at different times in the cell cycle (top three panels). Cells were also stained with anti-centrosome antibody in combination with blocked anti-amino-terminal Cul1 antibodies ( bottom panel). Cells were visualized and photographed as described (see Materials and Methods). ( B ) Cul1 localizes to the midbody. ( Left and middle ) NIH-3T3 cells were grown on coverslips, fixed in methanol, and labeled with affinity-purified rabbit anti-amino-terminal Cul1 antibodies ( left ) or affinity-purified rabbit anti-carboxy-terminal Cul1 antibodies followed by secondary antibodies( middle ). ( Right ) NIH-3T3 cells expressing Myc-tagged Cul1 were fixed as above and labeled with anti-Myc mAb 9E10 followed by secondary antibodies. ( C ) Immunoblotting also demonstrates that Cul1 is present at the centrosome. Samples as indicated: (Lane 1 ) Sf9 cell extract; (lane 2 ) insect cell extract [Hi5] expressing human Cul1; (lane 3 ) NIH-3T3 cell lysate; (lane 4 ) nuclei prepared from CHO cells; and (lane 5 ) centrosomes purified from CHO cells were subjected to Western blotting with affinity-purified rabbit antibodies to the amino-terminal region of Cul1 followed by HRP-conjugated secondary antibodies. Bands were detected using ECL reagents (Amersham). Two forms of Cul1 detected are indicated (arrows). Positions of migration of molecular mass markers are also indicated. Note also that whole-cell lysate from CHO cells gave a similar result as did 3T3 cell lysate (data not shown). ( D ) Immunoblotting demonstrates that Cul1 is NEDD8-modified. Rabbit affinity-purified anti-Cul1 ( left ) and rabbit anti-NEDD8 ( right ) immunoblots of partially purified Xenopus egg extract (lanes 1 ), and immunoprecipitates from the same partially purified extract using control normal mouse serum (lanes 2 ), or mouse anti-Cul1 antibodies (lanes 3 ). Bands were detected using ECL reagents (Amersham). Two forms of Cul1 and positions of migration of molecular mass markers are indicated.
    Figure Legend Snippet: A Nedd8-modified form of Cul1 is present at the centrosome. ( A ) NIH-3T3 cells were grown on cover slips, fixed in methanol and labeled with affinity-purified antibodies against the amino-terminal portion of human Cul1 and with human anti-centrosome antiserum, followed by secondary antibodies and Hoechst dye. Cul1 staining is shown at the centrosome at different times in the cell cycle (top three panels). Cells were also stained with anti-centrosome antibody in combination with blocked anti-amino-terminal Cul1 antibodies ( bottom panel). Cells were visualized and photographed as described (see Materials and Methods). ( B ) Cul1 localizes to the midbody. ( Left and middle ) NIH-3T3 cells were grown on coverslips, fixed in methanol, and labeled with affinity-purified rabbit anti-amino-terminal Cul1 antibodies ( left ) or affinity-purified rabbit anti-carboxy-terminal Cul1 antibodies followed by secondary antibodies( middle ). ( Right ) NIH-3T3 cells expressing Myc-tagged Cul1 were fixed as above and labeled with anti-Myc mAb 9E10 followed by secondary antibodies. ( C ) Immunoblotting also demonstrates that Cul1 is present at the centrosome. Samples as indicated: (Lane 1 ) Sf9 cell extract; (lane 2 ) insect cell extract [Hi5] expressing human Cul1; (lane 3 ) NIH-3T3 cell lysate; (lane 4 ) nuclei prepared from CHO cells; and (lane 5 ) centrosomes purified from CHO cells were subjected to Western blotting with affinity-purified rabbit antibodies to the amino-terminal region of Cul1 followed by HRP-conjugated secondary antibodies. Bands were detected using ECL reagents (Amersham). Two forms of Cul1 detected are indicated (arrows). Positions of migration of molecular mass markers are also indicated. Note also that whole-cell lysate from CHO cells gave a similar result as did 3T3 cell lysate (data not shown). ( D ) Immunoblotting demonstrates that Cul1 is NEDD8-modified. Rabbit affinity-purified anti-Cul1 ( left ) and rabbit anti-NEDD8 ( right ) immunoblots of partially purified Xenopus egg extract (lanes 1 ), and immunoprecipitates from the same partially purified extract using control normal mouse serum (lanes 2 ), or mouse anti-Cul1 antibodies (lanes 3 ). Bands were detected using ECL reagents (Amersham). Two forms of Cul1 and positions of migration of molecular mass markers are indicated.

    Techniques Used: Modification, Labeling, Affinity Purification, Staining, Expressing, Purification, Western Blot, Migration

    4) Product Images from "dCIP4 (Drosophila Cdc42-Interacting Protein 4) Restrains Synaptic Growth by Inhibiting the Secretion of the Retrograde Glass Bottom Boat Signal"

    Article Title: dCIP4 (Drosophila Cdc42-Interacting Protein 4) Restrains Synaptic Growth by Inhibiting the Secretion of the Retrograde Glass Bottom Boat Signal

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.0256-10.2010

    dCIP4 and Wsp inhibit Gbb secretion. A1–D2 , Confocal images of NMJs 6/7 stained for extracellular Gbb-GFP (red) and HRP (blue) in BG57-GAL4 /+ ( A1 , A2 ), BG57-GAL4 / UAS-gbb-GFP ( B1 , B2 ), BG57-GAL4,Df(3L)ED4342 / UAS-gbb-GFP,dcip4 1 ( C1 , C2 ), and BG57-GAL4
    Figure Legend Snippet: dCIP4 and Wsp inhibit Gbb secretion. A1–D2 , Confocal images of NMJs 6/7 stained for extracellular Gbb-GFP (red) and HRP (blue) in BG57-GAL4 /+ ( A1 , A2 ), BG57-GAL4 / UAS-gbb-GFP ( B1 , B2 ), BG57-GAL4,Df(3L)ED4342 / UAS-gbb-GFP,dcip4 1 ( C1 , C2 ), and BG57-GAL4

    Techniques Used: Staining

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    Incubation:

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    Article Snippet: After washing with phosphate buffered saline (PBS)/0·05% Tween and blocking with phosphate-buffered saline/gelatin 1%, plates were incubated for 1 hr with the supernatants of the cultured cells. .. After washing, plates were incubated for 1 hr with peroxidase-conjugated fragment goat anti-human IgA, IgG or IgM antibodies (Jackson ImmunoResearch). .. The assay was developed with o -phenylendiamine tablets (Sigma, St Louis, MO) as a chromogenic substrate.

    Article Title: Reduced numbers of switched memory B cells with high terminal differentiation potential in Down syndrome
    Article Snippet: After washing with PBS containing 0.05% Tween and blocking with PBS containing 1% gelatin (1 h, room temperature), plates were incubated for 1 h at 37°C with the supernatants of the cultured cells. .. After washing, plates were incubated for 1 h with peroxidase-conjugated fragment goat anti-human IgA or IgG or IgM antibodies (Jackson ImmunoResearch Laboratories). .. The assay was developed with O -phenylendiamine tablets (Sigma-Aldrich) as a chromogenic substrate.

    Article Title: Characterization of neutralizing versus binding antibodies and memory B cells in COVID-19 recovered individuals from India
    Article Snippet: The plates were washed extensively with PBS containing 0.05% Tween-20. .. After incubation, the plates were washed and the SARS-CoV-2 RBD specific IgG, IgM, IgA signals were detected by incubating with horseradish peroxidase (HRP) conjugated - anti-human IgG (Jackson ImmunoResearch Labs, #109-036-098), IgM (Jackson ImmunoResearch Labs, #109-036-129), or IgA (Jackson ImmunoResearch Labs, #109-036-011). .. Plates were then washed thoroughly and developed with o-phenylenediamine (OPD) substrate (Sigma, #P8787) in 0.05 M phosphate-citrate buffer (Sigma, #P4809) pH 5.0, containing with 0.012% hydrogen peroxide (Fisher Scientific, #18755) just before use.

    Article Title: Novel prokaryotic expression of thioredoxin-fused insulinoma associated protein tyrosine phosphatase 2 (IA-2), its characterization and immunodiagnostic application
    Article Snippet: After 3 washing steps with 0.05 % v/v Tween 20 in TBS (TBS-T) membranes were incubated ON at RT with polyclonal sera to Trx or IA-2 diluted 1/100 in 3 % w/v skim milk, 0.05 % v/v Tween 20 in TBS (TBS-MT), and then washed five times with TBS-T. .. Bound antibodies were visualized by incubation with peroxidase-conjugated goat antibodies to rabbit IgG (Jackson ImmunoResearch Laboratories, Inc., West Grove, PA) diluted 1/2000 in TBS-MT, followed by the addition of alpha-chloronaphthol (Sigma-Aldrich, Inc., St Louis, MO) and 10 vol H2 O2 . ..

    Article Title: Infant rhesus macaques as a non-human primate model of Bordetella pertussis infection
    Article Snippet: Microplates (96-well) were coated with the antigens PT, FHA, PRN, and/or ACT at 3 μg/mL and incubated at 4 °C overnight. .. Then, the plates were blocked with 3% (w/v) bovine serum albumin (BSA, Amresco, A0332) in phosphate-buffered saline (PBS) at 37 °C for 2 h. Diluted serum or NPW was added to each microplate and incubated at 37 °C for 1 h. After washing, horseradish peroxidase (HRP)-labelled sheep anti-monkey IgG (Invitrogen, USA, PA1–84631) or anti-human IgA (Jackson ImmunoResearch Laboratories, USA, 109–036-011) was added to the microplate, and the plate was incubated at 37 °C for 1 h. All of the ELISA plates were developed using tetramethylbenzidine (TMB; Solarbio, CHN, PR1200) to generate a colorimetric reaction, and the reaction was terminated with 2 mol/L H2 SO4. .. For each set of ELISA plates subjected to IgG detection, a pertussis antiserum WHO international standard was used as a reference (NIBSC code: 06/140).

    Article Title: Characterization of neutralizing versus binding antibodies and memory B cells in COVID-19 recovered individuals from India
    Article Snippet: The plates were washed extensively with PBS containing 0.05% Tween-20. .. After incubation, the plates were washed and the SARS-CoV-2 RBD specific IgG, IgM, IgA signals were detected by incubating with horseradish peroxidase (HRP) conjugated - anti-human IgG (Jackson ImmunoResearch Labs, #109-036-098), IgM (Jackson ImmunoResearch Labs, #109-036-129), or IgA (Jackson ImmunoResearch Labs, #109-036-011). .. Plates were then washed thoroughly and developed with o-phenylenediamine (OPD) substrate (Sigma, #P8787) in 0.05M phosphate-citrate buffer (Sigma, #P4809) pH 5.0, containing with 0.012% hydrogen peroxide (Fisher Scientific, #18755) just before use.

    Enzyme-linked Immunosorbent Assay:

    Article Title: Infant rhesus macaques as a non-human primate model of Bordetella pertussis infection
    Article Snippet: Microplates (96-well) were coated with the antigens PT, FHA, PRN, and/or ACT at 3 μg/mL and incubated at 4 °C overnight. .. Then, the plates were blocked with 3% (w/v) bovine serum albumin (BSA, Amresco, A0332) in phosphate-buffered saline (PBS) at 37 °C for 2 h. Diluted serum or NPW was added to each microplate and incubated at 37 °C for 1 h. After washing, horseradish peroxidase (HRP)-labelled sheep anti-monkey IgG (Invitrogen, USA, PA1–84631) or anti-human IgA (Jackson ImmunoResearch Laboratories, USA, 109–036-011) was added to the microplate, and the plate was incubated at 37 °C for 1 h. All of the ELISA plates were developed using tetramethylbenzidine (TMB; Solarbio, CHN, PR1200) to generate a colorimetric reaction, and the reaction was terminated with 2 mol/L H2 SO4. .. For each set of ELISA plates subjected to IgG detection, a pertussis antiserum WHO international standard was used as a reference (NIBSC code: 06/140).

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  • 86
    Jackson Immuno hrp conjugated donkey anti goat igg
    Analysis of sequence homology of V L and V H genes and purified anti-TS scFv antibodies. (A) Thirty scFv clones (15 containing short linker and 15 long linkers) were chosen after 4 th biopanning and determined their nucleotide sequences. The deduced amino acid sequences using the BioEdit program were compared to that of the chicken’s germline gene. Sequence gaps were launched with blank spaces to optimize the alignment. The dashes (-) represent the same amino acid sequences. Arrows on top of amino acid sequences of germline represent the domains of framework regions (FRs) and complementarity-determining regions (CDRs). (B) After adding IPTG for induction, His-fused scFvs (lanes TSS1 to TSL8) with binding activities to TS proteins using Ni 2+ Sepharose were purified and analyzed their purity on SDS-PAGE stained with Coomassie blue dye. (C) Their identities were further verified using goat anti-chicken light chain antibody, followed by <t>HRP-tagged</t> donkey anti-goat <t>IgG</t> on Western blots. Approximately 0.1 μg of each scFv antibody was used for analysis.
    Hrp Conjugated Donkey Anti Goat Igg, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hrp conjugated donkey anti goat igg/product/Jackson Immuno
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    Jackson Immuno hrp conjugated secondary antibodies
    Independent diffusion of SV proteins following nerve stimulation is sustained for long periods following LAP inactivation Third instar larval NMJ preparations from the indicated genotypes were dissected, incubated with FlAsH-EDT 2 and muscle 4 from segment A2 or A3 was exposed to 488-nm-filtered fluorescent light for 5 min. Clap4C; lap = Clap4C; lap 1 /lap sd3 . Following illumination, the larval NMJs were stimulated continuously with high K + (90 m m ) Jan's solution for 5 min (A and B) or 30 min (C and D) or 10 min (E and F). Following nerve stimulation, the larvae were washed rapidly with Ca 2+ -free HL-3 saline and fixed. The NMJs were then stained for a pair of SV proteins Syn and vGlut or Syt1 and <t>CSP.</t> Panels A–D also show <t>HRP-stained</t> NMJs (blue) to mark the neuronal membrane. The stimulation paradigm does not affect SV protein colocalization in wild-type control larval NMJs in which most SV proteins are colocalized although we note that not all SV proteins are fully colocalized even in the wild-type larval NMJs. In contrast, there are more punctate in LAP-inactivated synaptic boutons and SV proteins are often not colocalized in these punctate (arrows). G and H) Following 10 min of stimulation with high K + , nerve terminals were allowed to rest in Ca 2+ -free HL-3 saline for an additional 20 min prior to fixation. Following the resting period, dramatically large punctate can be observed positive for both Syt1 and Syn (arrowheads) in larval NMJs whose LAP is inactivated, while some portions of the punctate within the bouton are positive for only one of the two SV proteins (arrows). The protocol for both control and experimental samples was identical. Scale bars = 10 µm.
    Hrp Conjugated Secondary Antibodies, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hrp conjugated secondary antibodies/product/Jackson Immuno
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hrp conjugated secondary antibodies - by Bioz Stars, 2021-07
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    Jackson Immuno peroxidase hrp conjugated anti mouse immunoglobulin g igg
    Palytoxin (PLTX) binding evaluated on a panel of different cell lines, detected by a monoclonal mouse anti-PLTX antibody targeted by horseradish peroxidase <t>(HRP)-conjugated</t> anti-mouse immunoglobulin G. ( A ) Saturation curves of PLTX binding. Box plots showing ( B ) distribution of Kd values and ( C ) maximal bindings obtained by the binding assay for PLTX. Results are expressed as mean ± SE of three experiments performed in triplicate.
    Peroxidase Hrp Conjugated Anti Mouse Immunoglobulin G Igg, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Jackson Immuno secondary hrp conjugated donkey anti rabbit antibodies
    Determination of the coronavirus RTC-proximal proteome. ( a ) Schematic overview of the BirA R118G -mediated proximity biotinylation assay using MHV-BirA R118G -nsp2. ( b ) Western blot analysis of MHV-BirA R118G -nsp2-infected L929 cells. L929 cells were infected with MHV-BirA R118G -nsp2, MHV-A59 or non-infected in medium with and without supplementation of 67 µM biotin. Cells were lysed 15 h.p.i. and biotinylated factors were subjected to affinity purification using streptavidin-coupled magnetic beads. Total cell lysates and affinity-purified fractions were separated by SDS-PAGE and analysed by western blot probed with horse radish peroxidase <t>(HRP)-coupled</t> Streptavidin. ( c ) Host and viral factors identified by LC-MS/MS. 4*10 7 L929 cells were infected with MHV-BirA R118G -nsp2 or MHV-A59 in medium supplemented with 67 µM biotin. 15 h.p.i., lysates were affinity purified and LC-MS/MS was performed from in-gel digested samples. MS identification of biotinylated proteins was performed in three independent biological replicates. Spectral interpretation was performed against a Mus musculus and MHV database and log 2 -transformed LFQ levels (x-axis) were used to determine significant differences in protein enrichment between sample groups (Student's T-test, y-axis). Identified cellular proteins are displayed as black dots, MHV proteins are highlighted in red (nsp: non-structural protein, N: nucleocapsid, S: spike, M: membrane, 2a: accessory protein 2a). ( d ) Summary of viral proteins identified by LC-MS/MS. nsp2-10, nsp12-16, and nucleocapsid were significantly enriched in fractions derived from MHV-BirA R118G -nsp2-infected cells whereas nsp1, nsp11, structural proteins spike ( S ), envelope ( E ) and membrane proteins ( M ) as well as all accessory proteins (NS2a, HE, ORF4, ORF5a) were either not significantly enriched or not detected. ( e,f ) Immunofluorescence analysis of RTC-proximal cellular factors. L929 cells were seeded on coverslips, infected with MHV-BirA R118G -nsp2 ( e ) or MHV-A59 ( f ), fixed at 9 h.p.i. and processed for immunofluorescence using anti-myc, anti-RTN4 and <t>anti-eIF3E</t> antibodies ( e ) or anti-dsRNA, anti-RTN4 and anti-eIF3E antibodies ( f ). Secondary fluorophore-coupled antibodies were used to detect the viral replicase and endogenous levels of RTN4 and eIF3E ( e ). Scale bars: 10 µm; insets 5 µm. Proximity ligations were performed using Duolink In Situ detection reagents ( f ). Nuclei are counterstained with DAPI. Z-projection of deconvolved z-stacks acquired with a DeltaVision Elite High-Resolution imaging system are shown. Intensity profiles highlighted in the magnified regions are shown. Scale bars: 20 µm (insets 5 µm).
    Secondary Hrp Conjugated Donkey Anti Rabbit Antibodies, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Analysis of sequence homology of V L and V H genes and purified anti-TS scFv antibodies. (A) Thirty scFv clones (15 containing short linker and 15 long linkers) were chosen after 4 th biopanning and determined their nucleotide sequences. The deduced amino acid sequences using the BioEdit program were compared to that of the chicken’s germline gene. Sequence gaps were launched with blank spaces to optimize the alignment. The dashes (-) represent the same amino acid sequences. Arrows on top of amino acid sequences of germline represent the domains of framework regions (FRs) and complementarity-determining regions (CDRs). (B) After adding IPTG for induction, His-fused scFvs (lanes TSS1 to TSL8) with binding activities to TS proteins using Ni 2+ Sepharose were purified and analyzed their purity on SDS-PAGE stained with Coomassie blue dye. (C) Their identities were further verified using goat anti-chicken light chain antibody, followed by HRP-tagged donkey anti-goat IgG on Western blots. Approximately 0.1 μg of each scFv antibody was used for analysis.

    Journal: The Journal of Venomous Animals and Toxins Including Tropical Diseases

    Article Title: Chicken antibodies against venom proteins of Trimeresurus stejnegeri in Taiwan

    doi: 10.1590/1678-9199-JVATITD-2020-0056

    Figure Lengend Snippet: Analysis of sequence homology of V L and V H genes and purified anti-TS scFv antibodies. (A) Thirty scFv clones (15 containing short linker and 15 long linkers) were chosen after 4 th biopanning and determined their nucleotide sequences. The deduced amino acid sequences using the BioEdit program were compared to that of the chicken’s germline gene. Sequence gaps were launched with blank spaces to optimize the alignment. The dashes (-) represent the same amino acid sequences. Arrows on top of amino acid sequences of germline represent the domains of framework regions (FRs) and complementarity-determining regions (CDRs). (B) After adding IPTG for induction, His-fused scFvs (lanes TSS1 to TSL8) with binding activities to TS proteins using Ni 2+ Sepharose were purified and analyzed their purity on SDS-PAGE stained with Coomassie blue dye. (C) Their identities were further verified using goat anti-chicken light chain antibody, followed by HRP-tagged donkey anti-goat IgG on Western blots. Approximately 0.1 μg of each scFv antibody was used for analysis.

    Article Snippet: The bound anti-TS scFv antibodies were detected by adding a goat anti-chicken light chain (Bethyl, Laboratories, Montgomery, TX, USA); as the secondary antibody, followed by HRP-conjugated donkey anti-goat IgG (Jackson ImmunoResearch, West Grove, PA, USA) as the third antibody.

    Techniques: Sequencing, Purification, Clone Assay, Binding Assay, SDS Page, Staining, Western Blot

    Independent diffusion of SV proteins following nerve stimulation is sustained for long periods following LAP inactivation Third instar larval NMJ preparations from the indicated genotypes were dissected, incubated with FlAsH-EDT 2 and muscle 4 from segment A2 or A3 was exposed to 488-nm-filtered fluorescent light for 5 min. Clap4C; lap = Clap4C; lap 1 /lap sd3 . Following illumination, the larval NMJs were stimulated continuously with high K + (90 m m ) Jan's solution for 5 min (A and B) or 30 min (C and D) or 10 min (E and F). Following nerve stimulation, the larvae were washed rapidly with Ca 2+ -free HL-3 saline and fixed. The NMJs were then stained for a pair of SV proteins Syn and vGlut or Syt1 and CSP. Panels A–D also show HRP-stained NMJs (blue) to mark the neuronal membrane. The stimulation paradigm does not affect SV protein colocalization in wild-type control larval NMJs in which most SV proteins are colocalized although we note that not all SV proteins are fully colocalized even in the wild-type larval NMJs. In contrast, there are more punctate in LAP-inactivated synaptic boutons and SV proteins are often not colocalized in these punctate (arrows). G and H) Following 10 min of stimulation with high K + , nerve terminals were allowed to rest in Ca 2+ -free HL-3 saline for an additional 20 min prior to fixation. Following the resting period, dramatically large punctate can be observed positive for both Syt1 and Syn (arrowheads) in larval NMJs whose LAP is inactivated, while some portions of the punctate within the bouton are positive for only one of the two SV proteins (arrows). The protocol for both control and experimental samples was identical. Scale bars = 10 µm.

    Journal: Traffic (Copenhagen, Denmark)

    Article Title: AP180 Couples Protein Retrieval to Clathrin-Mediated Endocytosis of Synaptic Vesicles

    doi: 10.1111/tra.12153

    Figure Lengend Snippet: Independent diffusion of SV proteins following nerve stimulation is sustained for long periods following LAP inactivation Third instar larval NMJ preparations from the indicated genotypes were dissected, incubated with FlAsH-EDT 2 and muscle 4 from segment A2 or A3 was exposed to 488-nm-filtered fluorescent light for 5 min. Clap4C; lap = Clap4C; lap 1 /lap sd3 . Following illumination, the larval NMJs were stimulated continuously with high K + (90 m m ) Jan's solution for 5 min (A and B) or 30 min (C and D) or 10 min (E and F). Following nerve stimulation, the larvae were washed rapidly with Ca 2+ -free HL-3 saline and fixed. The NMJs were then stained for a pair of SV proteins Syn and vGlut or Syt1 and CSP. Panels A–D also show HRP-stained NMJs (blue) to mark the neuronal membrane. The stimulation paradigm does not affect SV protein colocalization in wild-type control larval NMJs in which most SV proteins are colocalized although we note that not all SV proteins are fully colocalized even in the wild-type larval NMJs. In contrast, there are more punctate in LAP-inactivated synaptic boutons and SV proteins are often not colocalized in these punctate (arrows). G and H) Following 10 min of stimulation with high K + , nerve terminals were allowed to rest in Ca 2+ -free HL-3 saline for an additional 20 min prior to fixation. Following the resting period, dramatically large punctate can be observed positive for both Syt1 and Syn (arrowheads) in larval NMJs whose LAP is inactivated, while some portions of the punctate within the bouton are positive for only one of the two SV proteins (arrows). The protocol for both control and experimental samples was identical. Scale bars = 10 µm.

    Article Snippet: Western blot Following dilution in SDS sample buffer, proteins were separated by SDS–PAGE, transferred to nitrocellulose and detected using the following antibodies: goat anti-LAP (1:2000); rabbit anti-vGlut (1:10 000, courtesy of Aaron DiAntonio, and this study); mouse anti-Syn (1:200); rabbit anti-Syt1 (1:1000, Noreen Reist); mouse anti-CSP (1:200, DSHB) and rabbit anti-nSyb (1:1000), followed by probing with HRP-conjugated secondary antibodies (1:1000, Jackson Immunoresearch).

    Techniques: Diffusion-based Assay, Incubation, Staining

    Palytoxin (PLTX) binding evaluated on a panel of different cell lines, detected by a monoclonal mouse anti-PLTX antibody targeted by horseradish peroxidase (HRP)-conjugated anti-mouse immunoglobulin G. ( A ) Saturation curves of PLTX binding. Box plots showing ( B ) distribution of Kd values and ( C ) maximal bindings obtained by the binding assay for PLTX. Results are expressed as mean ± SE of three experiments performed in triplicate.

    Journal: Toxins

    Article Title: A Novel Sensitive Cell-Based Immunoenzymatic Assay for Palytoxin Quantitation in Mussels

    doi: 10.3390/toxins10080329

    Figure Lengend Snippet: Palytoxin (PLTX) binding evaluated on a panel of different cell lines, detected by a monoclonal mouse anti-PLTX antibody targeted by horseradish peroxidase (HRP)-conjugated anti-mouse immunoglobulin G. ( A ) Saturation curves of PLTX binding. Box plots showing ( B ) distribution of Kd values and ( C ) maximal bindings obtained by the binding assay for PLTX. Results are expressed as mean ± SE of three experiments performed in triplicate.

    Article Snippet: The horseradish peroxidase (HRP)-conjugated anti-mouse immunoglobulin G (IgG) was purchased from Jackson ImmunoResearch (Newmarket, UK).

    Techniques: Binding Assay

    Determination of the coronavirus RTC-proximal proteome. ( a ) Schematic overview of the BirA R118G -mediated proximity biotinylation assay using MHV-BirA R118G -nsp2. ( b ) Western blot analysis of MHV-BirA R118G -nsp2-infected L929 cells. L929 cells were infected with MHV-BirA R118G -nsp2, MHV-A59 or non-infected in medium with and without supplementation of 67 µM biotin. Cells were lysed 15 h.p.i. and biotinylated factors were subjected to affinity purification using streptavidin-coupled magnetic beads. Total cell lysates and affinity-purified fractions were separated by SDS-PAGE and analysed by western blot probed with horse radish peroxidase (HRP)-coupled Streptavidin. ( c ) Host and viral factors identified by LC-MS/MS. 4*10 7 L929 cells were infected with MHV-BirA R118G -nsp2 or MHV-A59 in medium supplemented with 67 µM biotin. 15 h.p.i., lysates were affinity purified and LC-MS/MS was performed from in-gel digested samples. MS identification of biotinylated proteins was performed in three independent biological replicates. Spectral interpretation was performed against a Mus musculus and MHV database and log 2 -transformed LFQ levels (x-axis) were used to determine significant differences in protein enrichment between sample groups (Student's T-test, y-axis). Identified cellular proteins are displayed as black dots, MHV proteins are highlighted in red (nsp: non-structural protein, N: nucleocapsid, S: spike, M: membrane, 2a: accessory protein 2a). ( d ) Summary of viral proteins identified by LC-MS/MS. nsp2-10, nsp12-16, and nucleocapsid were significantly enriched in fractions derived from MHV-BirA R118G -nsp2-infected cells whereas nsp1, nsp11, structural proteins spike ( S ), envelope ( E ) and membrane proteins ( M ) as well as all accessory proteins (NS2a, HE, ORF4, ORF5a) were either not significantly enriched or not detected. ( e,f ) Immunofluorescence analysis of RTC-proximal cellular factors. L929 cells were seeded on coverslips, infected with MHV-BirA R118G -nsp2 ( e ) or MHV-A59 ( f ), fixed at 9 h.p.i. and processed for immunofluorescence using anti-myc, anti-RTN4 and anti-eIF3E antibodies ( e ) or anti-dsRNA, anti-RTN4 and anti-eIF3E antibodies ( f ). Secondary fluorophore-coupled antibodies were used to detect the viral replicase and endogenous levels of RTN4 and eIF3E ( e ). Scale bars: 10 µm; insets 5 µm. Proximity ligations were performed using Duolink In Situ detection reagents ( f ). Nuclei are counterstained with DAPI. Z-projection of deconvolved z-stacks acquired with a DeltaVision Elite High-Resolution imaging system are shown. Intensity profiles highlighted in the magnified regions are shown. Scale bars: 20 µm (insets 5 µm).

    Journal: eLife

    Article Title: Determination of host proteins composing the microenvironment of coronavirus replicase complexes by proximity-labeling

    doi: 10.7554/eLife.42037

    Figure Lengend Snippet: Determination of the coronavirus RTC-proximal proteome. ( a ) Schematic overview of the BirA R118G -mediated proximity biotinylation assay using MHV-BirA R118G -nsp2. ( b ) Western blot analysis of MHV-BirA R118G -nsp2-infected L929 cells. L929 cells were infected with MHV-BirA R118G -nsp2, MHV-A59 or non-infected in medium with and without supplementation of 67 µM biotin. Cells were lysed 15 h.p.i. and biotinylated factors were subjected to affinity purification using streptavidin-coupled magnetic beads. Total cell lysates and affinity-purified fractions were separated by SDS-PAGE and analysed by western blot probed with horse radish peroxidase (HRP)-coupled Streptavidin. ( c ) Host and viral factors identified by LC-MS/MS. 4*10 7 L929 cells were infected with MHV-BirA R118G -nsp2 or MHV-A59 in medium supplemented with 67 µM biotin. 15 h.p.i., lysates were affinity purified and LC-MS/MS was performed from in-gel digested samples. MS identification of biotinylated proteins was performed in three independent biological replicates. Spectral interpretation was performed against a Mus musculus and MHV database and log 2 -transformed LFQ levels (x-axis) were used to determine significant differences in protein enrichment between sample groups (Student's T-test, y-axis). Identified cellular proteins are displayed as black dots, MHV proteins are highlighted in red (nsp: non-structural protein, N: nucleocapsid, S: spike, M: membrane, 2a: accessory protein 2a). ( d ) Summary of viral proteins identified by LC-MS/MS. nsp2-10, nsp12-16, and nucleocapsid were significantly enriched in fractions derived from MHV-BirA R118G -nsp2-infected cells whereas nsp1, nsp11, structural proteins spike ( S ), envelope ( E ) and membrane proteins ( M ) as well as all accessory proteins (NS2a, HE, ORF4, ORF5a) were either not significantly enriched or not detected. ( e,f ) Immunofluorescence analysis of RTC-proximal cellular factors. L929 cells were seeded on coverslips, infected with MHV-BirA R118G -nsp2 ( e ) or MHV-A59 ( f ), fixed at 9 h.p.i. and processed for immunofluorescence using anti-myc, anti-RTN4 and anti-eIF3E antibodies ( e ) or anti-dsRNA, anti-RTN4 and anti-eIF3E antibodies ( f ). Secondary fluorophore-coupled antibodies were used to detect the viral replicase and endogenous levels of RTN4 and eIF3E ( e ). Scale bars: 10 µm; insets 5 µm. Proximity ligations were performed using Duolink In Situ detection reagents ( f ). Nuclei are counterstained with DAPI. Z-projection of deconvolved z-stacks acquired with a DeltaVision Elite High-Resolution imaging system are shown. Intensity profiles highlighted in the magnified regions are shown. Scale bars: 20 µm (insets 5 µm).

    Article Snippet: Membranes were blocked in 5% milk in PBS supplemented with 0.5% Tween20 (PBST) and incubated with primary antibodies (anti-eIF3E, HPA023973; anti-eIF3F, ab176853; anti-eIF3I, HPA029939) and secondary HRP-conjugated donkey anti-rabbit antibodies (Jackson ImmunoResearch) in 0.5% milk in PBST.

    Techniques: Cell Surface Biotinylation Assay, Western Blot, Infection, Affinity Purification, Magnetic Beads, SDS Page, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, Transformation Assay, Protein Enrichment, Derivative Assay, Immunofluorescence, In Situ, Imaging